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Protein

Pyruvate carboxylase 2

Gene

PYC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371ATPBy similarity
Binding sitei221 – 2211ATPBy similarity
Binding sitei256 – 2561ATPBy similarity
Active sitei313 – 3131By similarity
Metal bindingi567 – 5671Divalent metal cationBy similarity
Binding sitei639 – 6391SubstrateBy similarity
Metal bindingi735 – 7351Divalent metal cation; via carbamate groupBy similarity
Metal bindingi765 – 7651Divalent metal cationBy similarity
Metal bindingi767 – 7671Divalent metal cationBy similarity
Binding sitei899 – 8991SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. biotin carboxylase activity Source: InterPro
  3. DNA binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. pyruvate carboxylase activity Source: SGD

GO - Biological processi

  1. gluconeogenesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Biotin, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YBR218C-MONOMER.
BRENDAi6.4.1.1. 984.
ReactomeiREACT_188404. Defective HLCS causes multiple carboxylase deficiency.
REACT_188774. Biotin transport and metabolism.
REACT_235985. Gluconeogenesis.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase 2 (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase 2
Short name:
PCB 2
Gene namesi
Name:PYC2
Ordered Locus Names:YBR218C
ORF Names:YBR1507
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR218c.
SGDiS000000422. PYC2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11801179Pyruvate carboxylase 2PRO_0000146825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei735 – 7351N6-carboxylysineBy similarity
Modified residuei1136 – 11361N6-biotinyllysinePROSITE-ProRule annotationBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32327.
PaxDbiP32327.
PeptideAtlasiP32327.

Expressioni

Inductioni

By glucose.

Gene expression databases

GenevestigatoriP32327.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi32915. 88 interactions.
DIPiDIP-6426N.
IntActiP32327. 2 interactions.
MINTiMINT-2781496.
STRINGi4932.YBR218C.

Structurei

3D structure databases

ProteinModelPortaliP32327.
SMRiP32327. Positions 22-1170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 471453Biotin carboxylationAdd
BLAST
Domaini141 – 338198ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini558 – 825268CarboxyltransferaseAdd
BLAST
Domaini1095 – 117076Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni566 – 5705Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiCOG1038.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP32327.
KOiK01958.
OMAiLDYYLEV.
OrthoDBiEOG7GQZ41.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR18866:SF10. PTHR18866:SF10. 1 hit.
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY
60 70 80 90 100
SHEDRLSMHR LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH
110 120 130 140 150
PGYGFLSENS EFADKVVKAG ITWIGPPAEV IDSVGDKVSA RHLAARANVP
160 170 180 190 200
TVPGTPGPIE TVQEALDFVN EYGYPVIIKA AFGGGGRGMR VVREGDDVAD
210 220 230 240 250
AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG NVVHLFERDC
260 270 280 290 300
SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD
310 320 330 340 350
NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD
360 370 380 390 400
KITTRGFSIQ CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG
410 420 430 440 450
ATISPHYDSM LVKCSCSGST YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL
460 470 480 490 500
LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN RAQKLLHYLA DLAVNGSSIK
510 520 530 540 550
GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL LEKGPSEFAK
560 570 580 590 600
QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE
610 620 630 640 650
CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP
660 670 680 690 700
DNAIDHFVKQ AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC
710 720 730 740 750
YSGDMLQPGK KYNLDYYLEV VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI
760 770 780 790 800
GSLRTRYPDL PIHVHSHDSA GTAVASMTAC ALAGADVVDV AINSMSGLTS
810 820 830 840 850
QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC FEADLKGPDP
860 870 880 890 900
EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP
910 920 930 940 950
TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF
960 970 980 990 1000
PEPLRSDVLR NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS
1010 1020 1030 1040 1050
YNMYPRVYED FQKIRETYGD LSVLPTKNFL APAEPDEEIE VTIEQGKTLI
1060 1070 1080 1090 1100
IKLQAVGDLN KKTGQREVYF ELNGELRKIR VADKSQNIQS VAKPKADVHD
1110 1120 1130 1140 1150
THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV VSSPADGQVK
1160 1170 1180
DVFIKDGESV DASDLLVVLE EETLPPSQKK
Length:1,180
Mass (Da):130,167
Last modified:October 1, 1994 - v2
Checksum:iAD60DA3A60F5E001
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151S → C in CAA42544 (PubMed:1921979).Curated
Sequence conflicti132 – 1321D → E in CAA42544 (PubMed:1921979).Curated
Sequence conflicti238 – 2381N → K in CAA42544 (PubMed:1921979).Curated
Sequence conflicti268 – 2681L → F in CAA42544 (PubMed:1921979).Curated
Sequence conflicti546 – 5461S → C in CAA42544 (PubMed:1921979).Curated
Sequence conflicti642 – 6421N → T in CAA42544 (PubMed:1921979).Curated
Sequence conflicti771 – 7733GTA → STR in CAA42544 (PubMed:1921979).Curated
Sequence conflicti831 – 8311W → R in CAA42544 (PubMed:1921979).Curated
Sequence conflicti839 – 8391S → P in CAA42544 (PubMed:1921979).Curated
Sequence conflicti1001 – 10011Y → N in CAA42544 (PubMed:1921979).Curated
Sequence conflicti1155 – 11551K → R in CAA42544 (PubMed:1921979).Curated
Sequence conflicti1178 – 11781Q → P in CAA42544 (PubMed:1921979).Curated
Sequence conflicti1180 – 11801K → KVIFTR in CAA42544 (PubMed:1921979).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59890 Genomic DNA. Translation: CAA42544.1.
U35647 Genomic DNA. Translation: AAC49147.1.
Z36087 Genomic DNA. Translation: CAA85182.1.
BK006936 Genomic DNA. Translation: DAA07334.1.
PIRiS46094.
RefSeqiNP_009777.1. NM_001178566.1.

Genome annotation databases

EnsemblFungiiYBR218C; YBR218C; YBR218C.
GeneIDi852519.
KEGGisce:YBR218C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59890 Genomic DNA. Translation: CAA42544.1.
U35647 Genomic DNA. Translation: AAC49147.1.
Z36087 Genomic DNA. Translation: CAA85182.1.
BK006936 Genomic DNA. Translation: DAA07334.1.
PIRiS46094.
RefSeqiNP_009777.1. NM_001178566.1.

3D structure databases

ProteinModelPortaliP32327.
SMRiP32327. Positions 22-1170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32915. 88 interactions.
DIPiDIP-6426N.
IntActiP32327. 2 interactions.
MINTiMINT-2781496.
STRINGi4932.YBR218C.

Proteomic databases

MaxQBiP32327.
PaxDbiP32327.
PeptideAtlasiP32327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR218C; YBR218C; YBR218C.
GeneIDi852519.
KEGGisce:YBR218C.

Organism-specific databases

CYGDiYBR218c.
SGDiS000000422. PYC2.

Phylogenomic databases

eggNOGiCOG1038.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP32327.
KOiK01958.
OMAiLDYYLEV.
OrthoDBiEOG7GQZ41.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciYEAST:YBR218C-MONOMER.
BRENDAi6.4.1.1. 984.
ReactomeiREACT_188404. Defective HLCS causes multiple carboxylase deficiency.
REACT_188774. Biotin transport and metabolism.
REACT_235985. Gluconeogenesis.

Miscellaneous databases

NextBioi971553.

Gene expression databases

GenevestigatoriP32327.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR18866:SF10. PTHR18866:SF10. 1 hit.
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains."
    Stucka R., Dequin S., Salmon J.-M., Gancedo C.
    Mol. Gen. Genet. 229:307-315(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects on protein biotinylation."
    Val D.L., Chapman-Smith A., Walker M.E., Cronan J.E. Jr., Wallace J.C.
    Biochem. J. 312:817-825(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYC2_YEAST
AccessioniPrimary (citable) accession number: P32327
Secondary accession number(s): D6VQL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1994
Last modified: February 4, 2015
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.